The proposed research will investigate some of the biochemical and biophysical properties of structural proteins isolated from normal and cataractous human lenses. Gamma-crystallin, and other low molecular weight crystallins will be fractionated and characterized. The study will include: amino acid composition, molecular weight determination by ultracentrifugation and gel electrophoresis. Secondary and tertiary conformational parameters will be investigated by sensitive circular dichroism measurements. Effects of concentration, ionic strength, pH, and temperature on the conformation will be monitored by absorption, fluorescence, and circular dichroism measurements. The properties of proteins isolated from normal and cataractous lenses will be compared. The properties of fluorescent pigments found in normal and cataractous lenses will be studied by using absorption and fluorescence measurements on whole lenses, lens thin-sections and lens homogenate. Low temperature (77 degrees K) absorption spectra will be utilized to increase the resolution. Plasma membrane proteins will be isolated from normal and cataractous lenses. The study will include amino acid composition, molecular weight determination, and carbohydrate analysis. Structural studies using circular dichroism and laser Raman spectroscopy will be performed. The effects of various detergents on the conformation of the membrane proteins will be investigated.